메뉴 건너뛰기




Volumn 289, Issue 1, 2003, Pages 95-107

NUFIP1 (Nuclear FMRP Interacting Protein 1) is a nucleocytoplasmic shuttling protein associated with active synaptoneurosomes

Author keywords

Fragile X syndrome; Mental retardation; Nuclear export signal (NES); Nuclear matrix; RNA binding protein; Synaptoneurosomes

Indexed keywords

EXPORTIN 1; FRAGILE X MENTAL RETARDATION PROTEIN; PROTEIN; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 0041534394     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4827(03)00222-2     Document Type: Article
Times cited : (51)

References (61)
  • 3
    • 0033797832 scopus 로고    scopus 로고
    • Dendritic spine structural anomalies in Fragile-X mental retardation syndrome
    • Irwin S.A., Galvez R., Greenough W.T. Dendritic spine structural anomalies in Fragile-X mental retardation syndrome. Cereb. Cortex. 10:2000;1038-1044.
    • (2000) Cereb. Cortex , vol.10 , pp. 1038-1044
    • Irwin, S.A.1    Galvez, R.2    Greenough, W.T.3
  • 5
    • 0027176361 scopus 로고
    • The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation
    • Devys D., Lutz Y., Rouyer N., Bellocq J.P., Mandel J.L. The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation. Nat. Genet. 4:1993;335-340.
    • (1993) Nat. Genet. , vol.4 , pp. 335-340
    • Devys, D.1    Lutz, Y.2    Rouyer, N.3    Bellocq, J.P.4    Mandel, J.L.5
  • 6
    • 0026740718 scopus 로고
    • Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box
    • Kiledjian M., Dreyfuss G. Primary structure and binding activity of the hnRNP U protein binding RNA through RGG box . EMBO J. 11:1992;2655-2664.
    • (1992) EMBO J. , vol.11 , pp. 2655-2664
    • Kiledjian, M.1    Dreyfuss, G.2
  • 7
    • 0027273728 scopus 로고
    • The pre-mRNA binding K protein contains a novel evolutionary conserved motif
    • Siomi H., Matunis M.J., Michael W.M., Dreyfuss G. The pre-mRNA binding K protein contains a novel evolutionary conserved motif. Nucl. Acids Res. 21:1993;1193-1198.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 1193-1198
    • Siomi, H.1    Matunis, M.J.2    Michael, W.M.3    Dreyfuss, G.4
  • 8
    • 0029818460 scopus 로고    scopus 로고
    • A nuclear role for the Fragile X mental retardation protein
    • Fridell R.A., Benson R.E., Hua J., Bogerd H.P., Cullen B.R. A nuclear role for the Fragile X mental retardation protein. EMBO J. 15:1996;5408-5414.
    • (1996) EMBO J. , vol.15 , pp. 5408-5414
    • Fridell, R.A.1    Benson, R.E.2    Hua, J.3    Bogerd, H.P.4    Cullen, B.R.5
  • 9
    • 0029816723 scopus 로고    scopus 로고
    • The Fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals
    • Eberhart D.E., Malter H.E., Feng Y., Warren S.T. The Fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals. Hum. Mol. Genet. 5:1996;1083-1091.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1083-1091
    • Eberhart, D.E.1    Malter, H.E.2    Feng, Y.3    Warren, S.T.4
  • 10
    • 0031445652 scopus 로고    scopus 로고
    • Analysis of domains affecting intracellular localization of the FMRP protein
    • Bardoni B., Sittler A., Shen Y., Mandel J.L. Analysis of domains affecting intracellular localization of the FMRP protein. Neurobiol. Disease. 4:1997;329-336.
    • (1997) Neurobiol. Disease , vol.4 , pp. 329-336
    • Bardoni, B.1    Sittler, A.2    Shen, Y.3    Mandel, J.L.4
  • 12
    • 0031046778 scopus 로고    scopus 로고
    • Fragile X mental retardation protein: Nucleocytoplasmic shuttling and association with somatodendritic ribosomes
    • Feng Y., Gutekunst C.A., Eberhart D.E., Yi H., Warren S.T., Hersch S.M. Fragile X mental retardation protein nucleocytoplasmic shuttling and association with somatodendritic ribosomes . J. Neurosci. 17:1997;1539-1547.
    • (1997) J. Neurosci. , vol.17 , pp. 1539-1547
    • Feng, Y.1    Gutekunst, C.A.2    Eberhart, D.E.3    Yi, H.4    Warren, S.T.5    Hersch, S.M.6
  • 15
    • 0031310667 scopus 로고    scopus 로고
    • FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association
    • Feng Y., Absher D., Eberhart D.E., Brown V., Malter H.E., Warren S.T. FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association. Mol. Cell. 1:1997;109-118.
    • (1997) Mol. Cell , vol.1 , pp. 109-118
    • Feng, Y.1    Absher, D.2    Eberhart, D.E.3    Brown, V.4    Malter, H.E.5    Warren, S.T.6
  • 18
    • 0027377580 scopus 로고
    • FMR1 protein: Conserved RNP family domains and selective RNA binding
    • Ashley C.T. Jr., Wilkinson K.D., Reines D., Warren S.T. FMR1 protein conserved RNP family domains and selective RNA binding . Science. 262:1993;563-566.
    • (1993) Science , vol.262 , pp. 563-566
    • Ashley C.T., Jr.1    Wilkinson, K.D.2    Reines, D.3    Warren, S.T.4
  • 19
    • 0033499661 scopus 로고    scopus 로고
    • Isolation of an FMRP-associated messenger ribonucleoprotein particle and identification of nucleolin and the fragile X related proteins as components of the complex
    • Ceman S., Brown V., Warren S.T. Isolation of an FMRP-associated messenger ribonucleoprotein particle and identification of nucleolin and the fragile X related proteins as components of the complex. Mol. Cell. Biol. 19:1999;7925-7932.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7925-7932
    • Ceman, S.1    Brown, V.2    Warren, S.T.3
  • 20
    • 0035801393 scopus 로고    scopus 로고
    • The Fragile X mental retardation protein interacts specifically with its own mRNA via a purine-quartet structure
    • Schaeffer C., Bardoni B., Mandel J.L., Ehresmann B., Ehresmann C., Moine H. The Fragile X mental retardation protein interacts specifically with its own mRNA via a purine-quartet structure. EMBO J. 20:2001;4803-4813.
    • (2001) EMBO J. , vol.20 , pp. 4803-4813
    • Schaeffer, C.1    Bardoni, B.2    Mandel, J.L.3    Ehresmann, B.4    Ehresmann, C.5    Moine, H.6
  • 21
    • 0035900649 scopus 로고    scopus 로고
    • Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function
    • Darnell J.C., Jensen K.B., Jin P., Brown V., Warren S.T., Darnell R.B. Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function. Cell. 107:2001;489-499.
    • (2001) Cell , vol.107 , pp. 489-499
    • Darnell, J.C.1    Jensen, K.B.2    Jin, P.3    Brown, V.4    Warren, S.T.5    Darnell, R.B.6
  • 25
    • 0035368955 scopus 로고    scopus 로고
    • The fragile X mental retardation protein inhibits translation via interacting with mRNA
    • Li Z., Zhang Y., Ku L., Wilkinson K.D., Warren S.T., Feng Y. The fragile X mental retardation protein inhibits translation via interacting with mRNA. Nucl. Acids Res. 29:2001;2276-2283.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 2276-2283
    • Li, Z.1    Zhang, Y.2    Ku, L.3    Wilkinson, K.D.4    Warren, S.T.5    Feng, Y.6
  • 26
    • 0036591664 scopus 로고    scopus 로고
    • Advances in understanding of fragile X pathogenesis and FMRP function, and identification of X linked mental retardation genes
    • Bardoni B., Mandel J.L. Advances in understanding of fragile X pathogenesis and FMRP function, and identification of X linked mental retardation genes. Curr. Opin. Gen. Dev. 12:2002;284-293.
    • (2002) Curr. Opin. Gen. Dev. , vol.12 , pp. 284-293
    • Bardoni, B.1    Mandel, J.L.2
  • 29
    • 0032758839 scopus 로고    scopus 로고
    • A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein
    • Bardoni B., Schenck A., Mandel J.L. A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein. Hum. Mol. Genet. 8:1999;2557-2566.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2557-2566
    • Bardoni, B.1    Schenck, A.2    Mandel, J.L.3
  • 30
    • 0034731497 scopus 로고    scopus 로고
    • Identification of mouse YB1/p50 as a component of the FMRP-associated mRNP particles
    • Ceman S., Nelson R., Warren S.T. Identification of mouse YB1/p50 as a component of the FMRP-associated mRNP particles. Biochem. Biophys. Res. Comm. 279:2000;904-908.
    • (2000) Biochem. Biophys. Res. Comm. , vol.279 , pp. 904-908
    • Ceman, S.1    Nelson, R.2    Warren, S.T.3
  • 31
    • 0037020098 scopus 로고    scopus 로고
    • Identification of mRNA/protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor
    • Ohashi S., Koike K., Omori A., Ichinose S., Ohara S., Kobayashi S., Sato T.A., Anzai K. Identification of mRNA/protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor. J. Biol. Chem. 277:2002;37804-37810.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37804-37810
    • Ohashi, S.1    Koike, K.2    Omori, A.3    Ichinose, S.4    Ohara, S.5    Kobayashi, S.6    Sato, T.A.7    Anzai, K.8
  • 32
    • 0035902466 scopus 로고    scopus 로고
    • A highly conserved protein family interacting with the fragile X Mental Retardation Protein and displaying selective interactions with the FMRP related proteins FXR1P and FXR2P
    • Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.L. A highly conserved protein family interacting with the fragile X Mental Retardation Protein and displaying selective interactions with the FMRP related proteins FXR1P and FXR2P. Proc. Natl. Acad. Sci. USA. 98:2001;8844-8849.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8844-8849
    • Schenck, A.1    Bardoni, B.2    Moro, A.3    Bagni, C.4    Mandel, J.L.5
  • 34
    • 0025270026 scopus 로고
    • Core filaments of the nuclear matrix
    • He D., Nickerson A.D., Penman S. Core filaments of the nuclear matrix. J. Cell Biol. 110:1990;569-580.
    • (1990) J. Cell Biol. , vol.110 , pp. 569-580
    • He, D.1    Nickerson, A.D.2    Penman, S.3
  • 35
    • 0030971868 scopus 로고    scopus 로고
    • Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix
    • Reyes J.C., Muchardt C., Yaniv M. Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix. J. Cell Biol. 137:1997;263-274.
    • (1997) J. Cell Biol. , vol.137 , pp. 263-274
    • Reyes, J.C.1    Muchardt, C.2    Yaniv, M.3
  • 36
    • 0021675784 scopus 로고
    • Organization of the higher-order chromatin loop: Specific DNA attachment sites on nuclear scaffold
    • Mirkovitch J., Mirault M.-E., Laemmli U.K. Organization of the higher-order chromatin loop specific DNA attachment sites on nuclear scaffold . Cell. 39:1984;223-232.
    • (1984) Cell , vol.39 , pp. 223-232
    • Mirkovitch, J.1    Mirault, M.-E.2    Laemmli, U.K.3
  • 37
    • 0020420866 scopus 로고
    • Fine structure and localization of the nuclear matrix in situ
    • Brasch K. Fine structure and localization of the nuclear matrix in situ. Exp. Cell Res. 140:1982;161-171.
    • (1982) Exp. Cell Res. , vol.140 , pp. 161-171
    • Brasch, K.1
  • 38
    • 0024351482 scopus 로고
    • Electrophoretic analyses of nucleosomes and other proteins DNA-complexes
    • Huang S.Y., Garrard W.T. Electrophoretic analyses of nucleosomes and other proteins DNA-complexes. Methods Enzymol. 170:1989;116-142.
    • (1989) Methods Enzymol. , vol.170 , pp. 116-142
    • Huang, S.Y.1    Garrard, W.T.2
  • 39
    • 0033013469 scopus 로고    scopus 로고
    • The putative nuclear receptor mediator TIF1alpha is tightly associated with euchromatin
    • Remboutsika E., Lutz Y., Gansmuller A., Vonesch J.-L., Losson R., Chambon P. The putative nuclear receptor mediator TIF1alpha is tightly associated with euchromatin. J. Cell Sci. 112:1999;1671-1683.
    • (1999) J. Cell Sci. , vol.112 , pp. 1671-1683
    • Remboutsika, E.1    Lutz, Y.2    Gansmuller, A.3    Vonesch, J.-L.4    Losson, R.5    Chambon, P.6
  • 40
    • 0033396619 scopus 로고    scopus 로고
    • Visualization of synaptic activity in hippocampal slices with FM1-43 enabled by fluorescence quenching
    • Pyle J.L., Kavalali E.T., Choi S., Tsien R.W. Visualization of synaptic activity in hippocampal slices with FM1-43 enabled by fluorescence quenching. Neuron. 24:1999;803-808.
    • (1999) Neuron , vol.24 , pp. 803-808
    • Pyle, J.L.1    Kavalali, E.T.2    Choi, S.3    Tsien, R.W.4
  • 43
    • 0027499230 scopus 로고
    • Visualization of focal sites of transcription within human nuclei
    • Jackson D.A., Hassan B., Errington R., Cook P.R. Visualization of focal sites of transcription within human nuclei. EMBO J. 12:1993;1059-1065.
    • (1993) EMBO J. , vol.12 , pp. 1059-1065
    • Jackson, D.A.1    Hassan, B.2    Errington, R.3    Cook, P.R.4
  • 44
    • 0027305616 scopus 로고
    • Fluorescent labeling of nascent RNA reveals transcription by RNA polymerase II in domains scattered throughout the nucleus
    • Wansink D.G., Schul W., van der Kraan I., van Steensel B., van Driel R., de Jong L. Fluorescent labeling of nascent RNA reveals transcription by RNA polymerase II in domains scattered throughout the nucleus. J. Cell Biol. 122:1993;283-293.
    • (1993) J. Cell Biol. , vol.122 , pp. 283-293
    • Wansink, D.G.1    Schul, W.2    Van der Kraan, I.3    Van Steensel, B.4    Van Driel, R.5    De Jong, L.6
  • 45
    • 0033538831 scopus 로고    scopus 로고
    • Three dimensional visualization of transcription sites and their association with splicing factor-rich nuclear speckles
    • Wei X., Somanathan S., Samarabandu J., Berezney R. Three dimensional visualization of transcription sites and their association with splicing factor-rich nuclear speckles. J. Cell Biol. 146:1999;543-558.
    • (1999) J. Cell Biol. , vol.146 , pp. 543-558
    • Wei, X.1    Somanathan, S.2    Samarabandu, J.3    Berezney, R.4
  • 46
    • 0034083153 scopus 로고    scopus 로고
    • Orphan receptor DAX-1 is a shuttling RNA binding protein associated with polyribosomes via mRNA
    • Lalli E., Ohe K., Hindelang C., Sassone-Corsi P. Orphan receptor DAX-1 is a shuttling RNA binding protein associated with polyribosomes via mRNA. Mol. Cell. Biol. 20:2000;4910-4921.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4910-4921
    • Lalli, E.1    Ohe, K.2    Hindelang, C.3    Sassone-Corsi, P.4
  • 47
    • 0021255910 scopus 로고
    • Differentiation-dependent chromatin alterations precede and accompany transcription of immunoglobulin light chain genes
    • Rose S.M., Garrard W.T. Differentiation-dependent chromatin alterations precede and accompany transcription of immunoglobulin light chain genes. J. Biol. Chem. 259:1984;8534-8544.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8534-8544
    • Rose, S.M.1    Garrard, W.T.2
  • 48
    • 0022645387 scopus 로고
    • Activated murine alpha-globin gene is not preferentially associated with the nuclear matrix
    • Kirov N., Tsanev R. Activated murine alpha-globin gene is not preferentially associated with the nuclear matrix. Int. J. Biochem. 18:1986;155-159.
    • (1986) Int. J. Biochem. , vol.18 , pp. 155-159
    • Kirov, N.1    Tsanev, R.2
  • 49
    • 0014510120 scopus 로고
    • A new staining procedure for electron microscopical analysis
    • Bernhard W. A new staining procedure for electron microscopical analysis. J. Ultrastruct. Res. 27:1969;250-265.
    • (1969) J. Ultrastruct. Res. , vol.27 , pp. 250-265
    • Bernhard, W.1
  • 50
    • 0028158279 scopus 로고
    • Perichromatin fibrils are in situ forms of nascent transcripts
    • Fakan S. Perichromatin fibrils are in situ forms of nascent transcripts. Trends Cell Biol. 4:1994;86-90.
    • (1994) Trends Cell Biol. , vol.4 , pp. 86-90
    • Fakan, S.1
  • 51
    • 0026438715 scopus 로고
    • Intracellular movements of fluorescently labeled synaptic vesicles in frog motor nerve erminals during nerve stimulation
    • Betz W.J., Bewick G.S., Ridge R.M. Intracellular movements of fluorescently labeled synaptic vesicles in frog motor nerve erminals during nerve stimulation. Neuron. 9:1992;805-813.
    • (1992) Neuron , vol.9 , pp. 805-813
    • Betz, W.J.1    Bewick, G.S.2    Ridge, R.M.3
  • 52
    • 0028229610 scopus 로고
    • Inhibition of hippocampal heme oxygenase, nitric oxide synthetase and long-term potentiation by metalloporphyrins
    • Meffert M.K., Premack B.A., Schulman H. Inhibition of hippocampal heme oxygenase, nitric oxide synthetase and long-term potentiation by metalloporphyrins. Neuron. 12:1994;1235-1244.
    • (1994) Neuron , vol.12 , pp. 1235-1244
    • Meffert, M.K.1    Premack, B.A.2    Schulman, H.3
  • 53
    • 0033930208 scopus 로고    scopus 로고
    • Assembly of presynaptic active zones from cytoplasmic transport packets
    • Ahmari S.E., Buchanan J., Smith S.J. Assembly of presynaptic active zones from cytoplasmic transport packets. Nat. Neurosci. 3:2000;415-417.
    • (2000) Nat. Neurosci. , vol.3 , pp. 415-417
    • Ahmari, S.E.1    Buchanan, J.2    Smith, S.J.3
  • 54
    • 0039115156 scopus 로고    scopus 로고
    • Transport into and out of the cell nucleus
    • Görlich D. Transport into and out of the cell nucleus. EMBO J. 17:1998;2721-2727.
    • (1998) EMBO J. , vol.17 , pp. 2721-2727
    • Görlich, D.1
  • 55
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signal
    • Henderson B.R., Eleftheriou A. A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signal. Exp. Cell Res. 256:2000;213-224.
    • (2000) Exp. Cell Res. , vol.256 , pp. 213-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 56
    • 0034697158 scopus 로고    scopus 로고
    • Human ribosomal protein L5 contains defined nuclear localization and export signals
    • Rosorius O., Fries B., Stauber R.H., Hirschmann N., Bevec D., Hauber J. Human ribosomal protein L5 contains defined nuclear localization and export signals. J. Biol. Chem. 275:2000;12061-12068.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12061-12068
    • Rosorius, O.1    Fries, B.2    Stauber, R.H.3    Hirschmann, N.4    Bevec, D.5    Hauber, J.6
  • 57
    • 0033561446 scopus 로고    scopus 로고
    • Balancing import and export in development
    • Affolter M., Marty T., Vigano M.A. Balancing import and export in development. Genes Dev. 13:1999;913-915.
    • (1999) Genes Dev. , vol.13 , pp. 913-915
    • Affolter, M.1    Marty, T.2    Vigano, M.A.3
  • 59
    • 0028246435 scopus 로고
    • FMR1 knockout mice: A model to study fragile X mental retardation
    • FMR1 knockout mice a model to study fragile X mental retardation . Cell. 78:1994;23-33.
    • (1994) Cell , vol.78 , pp. 23-33
  • 60
    • 0030034421 scopus 로고    scopus 로고
    • A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into the polysomes
    • Visa N., Alzhanova-Ericsson A.L., Sun L., Kiseleva E., Björkroth B., Wurtz T., Daneholt B. A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into the polysomes. Cell. 84:1996;253-264.
    • (1996) Cell , vol.84 , pp. 253-264
    • Visa, N.1    Alzhanova-Ericsson, A.L.2    Sun, L.3    Kiseleva, E.4    Björkroth, B.5    Wurtz, T.6    Daneholt, B.7
  • 61
    • 0035912719 scopus 로고    scopus 로고
    • A cellular mechanism for targeting newly synthesized mRNAs to synaptic sites on dendrites
    • Steward O., Worley P.F. A cellular mechanism for targeting newly synthesized mRNAs to synaptic sites on dendrites. Proc. Natl. Acad. Sci. USA. 98:2001;7062-7068.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7062-7068
    • Steward, O.1    Worley, P.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.